ID A0A1R3T7L9_9BACT Unreviewed; 922 AA.
AC A0A1R3T7L9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=PSM36_1110 {ECO:0000313|EMBL:SCD19935.1};
OS Proteiniphilum saccharofermentans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Proteiniphilum.
OX NCBI_TaxID=1642647 {ECO:0000313|EMBL:SCD19935.1, ECO:0000313|Proteomes:UP000187464};
RN [1] {ECO:0000313|EMBL:SCD19935.1, ECO:0000313|Proteomes:UP000187464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3/6 {ECO:0000313|EMBL:SCD19935.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; LT605205; SCD19935.1; -; Genomic_DNA.
DR RefSeq; WP_076929528.1; NZ_LT605205.1.
DR AlphaFoldDB; A0A1R3T7L9; -.
DR STRING; 1642647.PSM36_1110; -.
DR KEGG; psac:PSM36_1110; -.
DR Proteomes; UP000187464; Chromosome i.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:SCD19935.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SCD19935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187464};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..922
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010221825"
FT DOMAIN 51..180
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 185..283
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 292..406
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 922 AA; 104920 MW; 91DC6DA661E7F88A CRC64;
MKKIILLCVS LLTFLSYGQQ TESLYLSGTG SDNTVLWDFF CTAGRKSGEW AKIPVPSNWE
FEGFGQFTYG HDKERINETG LYRHSFVLPE IWKGKQINIV FEGVMTDTEV KVNGQVAGEI
HQGGFYCFKY DITDLLKFGE DNLLEVTVHK SSSNESVENA ERKSDFWVYG GIYRPVWLEV
LPKEHIDRVA IDARCDGIFQ MDVFLSDNIG NAQVTAQVKT LEGKLFGNAI TANTDKSGIT
RLSAEFDNPK LWSSEFPNRY QVEVSLIKNG KNVHNITEKF GFRTAELRPG DGFYINGSRI
KFKGVNRHTH WPTTGRATSY SISLMDALLI KEMNMNAVRM SHYPPDRHFL DICDSLGLYV
IDELTGWQSM YDTEVGKKLV RELVVRDVNH PSIVMWANGN EGGFNFDLVP EYPKFDIQKR
HVFHPWLEEE YTNTYHYPAY GVGTNFLFNG NKLFFPTEFM HGLYDGGHGA GLDDFWNLIQ
FNPLGAGGFL WDLVDQGVVR SDRDNEIDTD GNHAADGIVG PFREKEGSFY TIKEIWSPVY
LEGTTFLPPS FDGVFRVQNR YHFTNLNQCS FTAKWINFDY LAGVKNELET DVSVADIPPG
FNGLIKVSLP EDISDYDALS LTATDIYGRE IHTWTRTITP ASRYALRLIE RENSIVKQEE
QNGEIILSSK DVRLVIDRTS GIIRQIESNG QRLSLTNGPR YTNGNMALDE LDKVVEDNLE
KIRLSFRDEN SSRPGRRNVI TLSLLPSGWI EIDYSFDVGG YHDHIGITFD YPEDKVKHVK
WLGNGPYRVW KNRMKGVSFN IWEKEYNNTI TGESWEYPEF KGFHSNLYAA DLATDEGILR
IVAASEDLFL HLFTPDNPVK RNNDNTLGVF PDGQLSILNA ISPVGTKFKQ AKELGPQSRQ
NYFLSSGHAE PLRGKVYLKF IP
//
